Recombinant Mouse EGFLAM Flag-tag Protein, CF

When Recombinant Human Dystroglycan Fc Chimera (Catalog # 10223-DG) is immobilized at 1 μg/mL (100 μL/well), the concentration of Recombinant Mouse EGFLAM Flag-tag Protein (Catalog # 10367-EG) binds with an ED50 of 0.075‑0.45 μg/mL.

2 μg/lane of Recombinant Mouse EGFLAM (Catalog # 10367-EG) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 103-198 kDa.

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse EGFLAM Flag-tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Dystroglycan Fc Chimera (Catalog # 10223-DG) is immobilized at 1 µg/mL (100 µL/well), Recombinant Mouse EGFLAM Flag-tag (Catalog # 10367-EG) binds with an ED₅₀ of 0.075-0.45 μg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived mouse EGFLAM protein
  

  Mouse EGFLAM (Leu25-Lys1017) Accession # Q4VBE4.1	DYKDDDDK (Flag-tag)	DYKDDDDK (Flag-tag)	DYKDDDDK (Flag-tag)
  N-terminus			C-terminus

• Accession #: Q4VBE4.1
• N-terminal Sequence: Leu25
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 111 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 103-198 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
• Buffer:
  Supplied as a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse EGFLAM Flag-tag Protein, CF

• AGRINL
• AGRINLAGRNLFLJ39155
• Agrin-like protein
• AGRNL
• EGFLAM
• EGF-like, fibronectin type III and laminin G domains
• EGF-like, fibronectin type-III and laminin G-like domain-containing protein
• PIKA
• Pikachurin

Background

EGFLAM (EGF-like, fibronectin type-III and laminin G-like domain-containing protein), also known as Pikachurin or Nectican, is a highly conserved extracellular matrix-like protein with a molecular weight around 110 kDa. Murine EGFLAM has 1,017 amino acids (∼110 kDa) with a 24 amino acids signal peptide. It can bind to alpha -dystroglycan and has been found to localize mainly in the synaptic cleft of photoreceptor ribbon synapses (1). At the ribbon synapses, EGFLAM protein is colocalized with both dystrophin and dystroglycan, where it plays critical roles in interactions between the photoreceptor ribbon synapse and bipolar dendrites (1, 2). EGFLAM gene is also expressed in other organs and tissues including brain, endocrine tissues and muscle tissues (3). EGFLAM has been considered as a new biomarker for theca interna and granulosa cells (4), a novel susceptibility locus for aortic aneurysm (3), a hypomethylated biomarkers for ovarian cancer (5), and a prognostic biomarker and therapeutic target for glioblastoma (6). EGFLAM contains 11 intracellular disulfide bonds and one O-glycosylation site that attaches to chondroitin sulfate and heparan sulfate. This protein is composed of two fibronectin type-III domains followed by three EGF-like domain and three Laminin G-like domains. Mouse EGFLAM shares 89% and 95% amino acid identity to human and rat EGFLAM, respectively.

1. Sato, S. et al. (2008) Nat. Neurosci. 11:923.
2. Han, J. and Townes-Anderson, E. (2012) PloS One 7:e50552.
3. Yamada, Y. et al. (2017) Int. J. Mol. Med. 39:1091.
4. Hatzirodos, N. et al. (2015) PLoS One 10:e0119800.
5. Gu, X.H. et al. (2009) Zhonghua Fu Chan Ke Za Zhi 44:754.
6. Chen, Juhui, et al. (2019) Cancer Biomarkers 24:343.

Bioinformatics

• Uniprot:
  • Q4VBE4.1()